1lm4: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
[[Image:1lm4.gif|left|200px]]
[[Image:1lm4.gif|left|200px]]


{{Structure
<!--
|PDB= 1lm4 |SIZE=350|CAPTION= <scene name='initialview01'>1lm4</scene>, resolution 1.45&Aring;
The line below this paragraph, containing "STRUCTURE_1lm4", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
|LIGAND= <scene name='pdbligand=CSW:CYSTEINE-S-DIOXIDE'>CSW</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide_deformylase Peptide deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.88 3.5.1.88] </span>
or leave the SCENE parameter empty for the default display.
|GENE= pdf1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus])
-->
|DOMAIN=
{{STRUCTURE_1lm4|  PDB=1lm4 |  SCENE= }}  
|RELATEDENTRY=[[1lm6|1LM6]], [[1lme|1LME]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lm4 OCA], [http://www.ebi.ac.uk/pdbsum/1lm4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lm4 RCSB]</span>
}}


'''Structure of Peptide Deformylase from Staphylococcus aureus at 1.45 A'''
'''Structure of Peptide Deformylase from Staphylococcus aureus at 1.45 A'''
Line 37: Line 34:
[[Category: Vincent, J.]]
[[Category: Vincent, J.]]
[[Category: Warner, I.]]
[[Category: Warner, I.]]
[[Category: metalloenzyme]]
[[Category: Metalloenzyme]]
[[Category: pdf]]
[[Category: Pdf]]
[[Category: staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:03:14 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:04:31 2008''

Revision as of 00:03, 3 May 2008

File:1lm4.gif

Template:STRUCTURE 1lm4

Structure of Peptide Deformylase from Staphylococcus aureus at 1.45 A


OverviewOverview

Peptide deformylase (PDF) has received considerable attention during the last few years as a potential target for a new type of antibiotics. It is an essential enzyme in eubacteria for the removal of the formyl group from the N terminus of the nascent polypeptide chain. We have solved the X-ray structures of four members of this enzyme family, two from the Gram-positive pathogens Streptococcus pneumoniae and Staphylococcus aureus, and two from the Gram-negative bacteria Thermotoga maritima and Pseudomonas aeruginosa. Combined with the known structures from the Escherichia coli enzyme and the recently solved structure of the eukaryotic deformylase from Plasmodium falciparum, a complete picture of the peptide deformylase structure and function relationship is emerging. This understanding could help guide a more rational design of inhibitors. A structure-based comparison between PDFs reveals some conserved differences between type I and type II enzymes. Moreover, our structures provide insights into the known instability of PDF caused by oxidation of the metal-ligating cysteine residue.

About this StructureAbout this Structure

1LM4 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

ReferenceReference

Structure analysis of peptide deformylases from Streptococcus pneumoniae, Staphylococcus aureus, Thermotoga maritima and Pseudomonas aeruginosa: snapshots of the oxygen sensitivity of peptide deformylase., Kreusch A, Spraggon G, Lee CC, Klock H, McMullan D, Ng K, Shin T, Vincent J, Warner I, Ericson C, Lesley SA, J Mol Biol. 2003 Jul 4;330(2):309-21. PMID:12823970 Page seeded by OCA on Sat May 3 00:03:14 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA